Nuclear magnetic resonance chemical shift: comparison of estimated secondary structures in peptides by nuclear magnetic resonance and circular dichroism
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چکیده
منابع مشابه
Circular dichroism and nuclear magnetic resonance spectroscopic analysis of immunogenic gluten peptides and their analogs.
Celiac Sprue, or gluten-sensitive enteropathy, is an inheritable human disease of the small intestine that is triggered by the dietary intake of gluten. Recently, several Pro- and Gln-rich peptide sequences (most notably PQPQLPY and analogs) have been identified from gluten with potent immunogenic activity toward CD4(+) T cells from small intestinal biopsies of Celiac Sprue patients. These pept...
متن کاملCircular Dichroism and Nuclear Magnetic Resonance Spectroscopic Analysis of Immunogenic Gluten Peptides and Their Analogs*□S
Celiac Sprue, or gluten-sensitive enteropathy, is an inheritable human disease of the small intestine that is triggered by the dietary intake of gluten. Recently, several Proand Gln-rich peptide sequences (most notably PQPQLPY and analogs) have been identified from gluten with potent immunogenic activity toward CD4 T cells from small intestinal biopsies of Celiac Sprue patients. These peptides ...
متن کاملNUCLEAR MAGNETIC RESONANCE STUDY OF THE STRUCTURE OF GLYOXALDIHYDRAZONE
Study of the nuclear magnetic resonance spectra of glyoxaldihydrazone in dimethylsulfoxide and deuterochlorofonn leads to the conclusion that this compound exists predominantly in non-chelate structure
متن کاملUsing Nuclear Magnetic Resonance
Quantum dense coding has been demonstrated experimentally in terms of quantum logic gates and circuits in quantum computation and NMR technique. Two bits of information has been transmitted through manipulating one of the maximally entangled two-state quantum pair, which is completely consistent with the original ideal of Bennett-Wiesner proposal. Although information transmission happens betwe...
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ژورنال
عنوان ژورنال: "Protein Engineering, Design and Selection"
سال: 1996
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/9.1.15